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Chloramphenicol is a broad-spectrum antibiotic that typically stops bacterial growth by stopping the production of proteins. [5] Chloramphenicol was discovered after being isolated from Streptomyces venezuelae in 1947. [8] Its chemical structure was identified and it was first synthesized in 1949.
Chloramphenicol Thiamphenicol. Amphenicols are a class of antibiotics with a phenylpropanoid structure. They function by blocking the enzyme peptidyl transferase on the 50S ribosome subunit of bacteria. [1] Examples of amphenicols include chloramphenicol, thiamphenicol, azidamfenicol, and florfenicol. The first-in-class compound was ...
Mildred Catherine Rebstock (November 29, 1919 – February 17, 2011) was an American pharmaceutical chemist.She and her team were the first to fully synthesize chloromycetin, also known as chloramphenicol.
Streptomyces venezuelae [1] is a species of soil-dwelling [2] Gram-positive bacterium of the genus Streptomyces. [3] S. venezuelae is filamentous.In its spore-bearing stage, hyphae perfuse both above ground as aerial hyphae and in the soil substrate. [3]
Chloramphenicol acetyltransferase (or CAT) is a bacterial enzyme (EC 2.3.1.28) [1] that detoxifies the antibiotic chloramphenicol and is responsible for chloramphenicol resistance in bacteria. [2] This enzyme covalently attaches an acetyl group from acetyl-CoA to chloramphenicol, which prevents chloramphenicol from binding to ribosomes .
The history of the tetracyclines involves the collective contributions of thousands of dedicated researchers, scientists, clinicians, and business executives. Tetracyclines were discovered in the 1940s, first reported in scientific literature in 1948, and exhibited activity against a wide range of microorganisms.
Unlike chloramphenicol, thiamphenicol is not readily metabolized in cattle, poultry, sheep, or humans, but is predominantly excreted unchanged. In pigs and rats the drug is excreted both as parent drug and as thiamphenicol glucuronate. [2] Thiamphenicol can be administered as a part of a complex molecule, Thiamphenicol glycinate acetylcysteine. [4]
Chloramphenicol binds [6] to residues A2451 and A2452 in the 23S rRNA of the ribosome and inhibits peptide bond formation. Pleuromutilins also bind to the peptidyl transferase center. [7] Macrolide antibiotics are thought to inhibit peptidyl transferase, in addition to inhibiting ribosomal translocation. [8]